ZRAB2_PIG
ID ZRAB2_PIG Reviewed; 328 AA.
AC Q19QU3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Zinc finger Ran-binding domain-containing protein 2;
DE AltName: Full=Zinc finger protein 265;
GN Name=ZRANB2; Synonyms=ZNF265;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16978188; DOI=10.1111/j.1365-2052.2006.01499.x;
RA Kim J.H., Lim H.T., Park E.W., Ovilo C., Lee J.H., Jeon J.T.;
RT "A gene-based radiation hybrid map of the pig chromosome 6q32 region
RT associated with a QTL for fat deposition traits.";
RL Anim. Genet. 37:522-523(2006).
CC -!- FUNCTION: Splice factor required for alternative splicing of
CC TRA2B/SFRS10 transcripts. May interfere with constitutive 5'-splice
CC site selection (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the C-terminal half of SNRNP70, the Arg/Ser-
CC rich domain of AKAP17A as well as with U2AF1 and CLK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The RanBP2-type zinc fingers mediate binding to RNA.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ZRANB2 family. {ECO:0000305}.
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DR EMBL; DQ499443; ABF72033.1; -; mRNA.
DR RefSeq; NP_001038047.1; NM_001044582.1.
DR AlphaFoldDB; Q19QU3; -.
DR SMR; Q19QU3; -.
DR STRING; 9823.ENSSSCP00000004096; -.
DR PaxDb; Q19QU3; -.
DR PeptideAtlas; Q19QU3; -.
DR PRIDE; Q19QU3; -.
DR Ensembl; ENSSSCT00070031607; ENSSSCP00070026351; ENSSSCG00070015892.
DR GeneID; 733651; -.
DR KEGG; ssc:733651; -.
DR CTD; 9406; -.
DR eggNOG; KOG1995; Eukaryota.
DR HOGENOM; CLU_061048_0_0_1; -.
DR InParanoid; Q19QU3; -.
DR OMA; DLWGDNE; -.
DR OrthoDB; 1399319at2759; -.
DR TreeFam; TF105996; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 6.
DR Genevisible; Q19QU3; SS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001530; F:lipopolysaccharide binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR InterPro; IPR017337; ZRANB2.
DR Pfam; PF00641; zf-RanBP; 2.
DR PIRSF; PIRSF037956; UCP037956_ZnF_Ran; 1.
DR SMART; SM00547; ZnF_RBZ; 2.
DR SUPFAM; SSF90209; SSF90209; 2.
DR PROSITE; PS01358; ZF_RANBP2_1; 2.
DR PROSITE; PS50199; ZF_RANBP2_2; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..328
FT /note="Zinc finger Ran-binding domain-containing protein 2"
FT /id="PRO_0000262915"
FT ZN_FING 9..40
FT /note="RanBP2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 65..94
FT /note="RanBP2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 117..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..328
FT /note="Required for nuclear targeting"
FT /evidence="ECO:0000250"
FT COMPBIAS 117..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95218"
FT MOD_RES 18
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R020"
FT MOD_RES 54
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95218"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R020"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95218"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95218"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95218"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95218"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95218"
SQ SEQUENCE 328 AA; 37111 MW; C842A783D1714F42 CRC64;
MSTKNFRVSD GDWICPDKKC GNVNFARRTS CNRCGREKTT EAKMMKAGGT EIGKTLAEKS
RGLFSANDWQ CKTCSNVNWA RRSECNMCNT PKYAKLEERT GYGGGFNERE NVEYIEREES
DGEYDEFGRK KKKYRGKAVG PASILKEVED KESEGEEEDE DEDLSKYKLD EDEDEDDADL
SKYNLDASEE EDSNKKKSNR RSRSKSRSSH SRSSSRSSSP SSSRSRSRSR SRSSSSSQSR
SRSTSRERSR SRGSKSSSRS HRGSSSPRKR SYSSSSSSPE RNRKRSRSRS SSTGDPKKRR
TRSRSPERHH RSSSGSSHSG SRSSSKKK
